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Volumn 40, Issue 7, 2001, Pages 2138-2147

A comparative study of peptide models of the α-domain of α-lactalbumin, lysozyme, and α-lactalbumin/lysozyme chimeras allows the elucidation of critical factors that contribute to the ability to form stable partially folded states

(6) Demarest, S J a Zhou, S Q a Robblee, J b Fairman, R b Chu, B a Raleigh, D P a

a STONY BROOK UNIVERSITY (United States)

b HAVERFORD COLLEGE (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA LACTALBUMIN; LYSOZYME;

ANIMAL CELL; ARTICLE; CHIMERA; CIRCULAR DICHROISM; CONTROLLED STUDY; CROSS LINKING; FLUORESCENCE; LIGHT SCATTERING; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION;

AMINO ACID SEQUENCE; ANIMALS; CHICKENS; CIRCULAR DICHROISM; DIMERIZATION; HUMANS; LACTALBUMIN; LIGHT; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MURAMIDASE; PEPTIDE FRAGMENTS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SCATTERING, RADIATION; SPECTROMETRY, FLUORESCENCE; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS; ULTRACENTRIFUGATION;

ANIMALIA;

EID: 0035916225 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi001975z Document Type: Article

Times cited : (12)

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